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Papers In Press, published online ahead of print May 30, 2002
Ludwig Institute for Cancer Research, University of California, San Diego, La Jolla, CA 92093-0669
Corresponding Author: rkolodner{at}ucsd.edu
The MER3 protein of Saccharomyces cerevisiae is required for crossing over in meiosis, and has been suggested to act at the initiation of homologous pairing and the resolution of Holliday junctions. The purified MER3 protein is a DNA helicase that translocates along single-stranded DNA (ssDNA) in the 3’ to 5’ direction displacing annealed DNA fragments. Here MER3 was found to be able to unwind various double-stranded DNA (dsDNA) substrates, including a 30-bp dsDNA with a 20-nt 3'-overhang, a 30-bp dsDNA with a 20-nt 5'-overhang, a 50-bp dsDNA with blunt ends, and a Holliday junction with 25-bp arms each of which had a blunt end. Efficient unwinding of the 3'-overhang substrate appeared to initiate by binding of MER3 to the 3'-single-stranded tail, in a reaction that required 6 or more unpaired bases. Unwinding of the blunt end and 5'-overhang substrates appeared to initiate at the blunt ends of these substrates. Unwinding of the Holliday junction was more efficient than unwinding of the blunt and 5’-overhang substrates, and was influenced by Mg2+ concentrations that cause changes in the structure of the junction. Possible roles for Holliday junction unwinding in meiotic crossing over are discussed.
J. Biol. Chem, 10.1074/jbc.M204165200
Submitted on April 29, 2002
Revised on May 28, 2002
Accepted on May 29, 2002
The MER3 DNA helicase catalyzes the unwinding of Holliday junctions
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